On the role of aromatic side chains in the photoactivation of BLUF domains

M.L. Gauden, J.S. Grinstead, W. Laan, H.M. van Stokkum, M. Avila-Perez, K.C. Toh, R. Boelens, R. Kaptein, R. van Grondelle, K.J. Hellingwerf, J.T.M. Kennis

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

BLUF (blue-light sensing using FAD) domain proteins are a novel group of blue-light sensing receptors found in many microorganisms. The role of the aromatic side chains Y21 and W104, which are in close vicinity to the FAD cofactor in the AppA BLUF domain from Rhodobacter sphaeroides, is investigated through the introduction of several amino acid substitutions at these positions. NMR spectroscopy indicated that in the W104F mutant, the local structure of the FAD binding pocket was not significantly perturbed as compared to that of the wild type. Time-resolved fluorescence and absorption spectroscopy was applied to explore the role of Y21 and W104 in AppA BLUF photochemistry. In the Y21 mutants, FADH
Original languageEnglish
Pages (from-to)7405-7415
JournalBiochemistry
Volume46
Issue number25
DOIs
Publication statusPublished - 2007

Bibliographical note

On the role of aromatic side chains in the photoactivation of BLUF domains

Fingerprint

Dive into the research topics of 'On the role of aromatic side chains in the photoactivation of BLUF domains'. Together they form a unique fingerprint.

Cite this